Why the study?
It remains unclear how pestivirus nonstructural proteins are functionalized for RNA replication versus virion formation, and the role of specific NS2 and accessory mutations has not been clarified.
The study identifies critical mutations in NS3/4A complexes that enable NS2-3-independent virion formation in pestiviruses, providing insights into viral genome packaging.
Hypothesis-generating in pestivirus models; extends mechanistic insights but leaves open relevance to human pathogens.
members, the nonstructural proteins are essential for virion formation and thus exert a dual role in RNA replication and virion morphogenesis. However, it remains unclear how these proteins are functionalized for either process. In wild-type pestiviruses, the NS3/4A complex is selectively active in RNA replication, while NS2-3/4A is essential for virion formation. Mutations recently identified in BVDV-1 rendered NS3/4A capable of supporting NS2-3-independent virion morphogenesis. A comparison of NS3/4A complexes incapable/capable of supporting virion morphogenesis revealed that changes in NS3/NS4A surface interactions are decisive for the gain of function. However, so far, the role of the NS2 mutations as well as the accessory mutations additionally required in the NS2-IRES-NS3 virus variant has not been clarified. To unravel the course of genome packaging, the additional sets of mutations obtained for a second pestivirus species (CSFV) are of significant importance to develop mechanistic models for this complex process.
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Dubrau et al. (2019) studied this question.
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